Heme ligase (EC 4.99.1.8, heme detoxification protein, HDP, hemozoin synthase) is an enzyme with systematic name Fe3+:ferriprotoporphyrin IX ligase (β-hematin-forming).[1] This enzyme catalyses the following reaction:
2 ferriprotoporphyrin IX beta-hematin
This heme detoxifying enzyme is found in Plasmodium parasites.
^Jani D, Nagarkatti R, Beatty W, Angel R, Slebodnick C, Andersen J, Kumar S, Rathore D (April 2008). "HDP-a novel heme detoxification protein from the malaria parasite". PLOS Pathogens. 4 (4): e1000053. doi:10.1371/journal.ppat.1000053. PMC 2291572. PMID 18437218.
Hemeligase (EC 4.99.1.8, heme detoxification protein, HDP, hemozoin synthase) is an enzyme with systematic name Fe3+:ferriprotoporphyrin IX ligase (β-hematin-forming)...
Photo, a graphics file format Health Device Profile, a Bluetooth profile Hemeligase, an enzyme Hierarchical decision process Hierarchical Dirichlet process...
enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic...
of genes encoding cytoprotective proteins. NRF2 induces the expression of heme oxygenase 1 in vitro leading to an increase in phase II enzymes. NRF2 also...
known as succinyl-CoA synthetase or succinate thiokinase or succinate-CoA ligase) is an enzyme that catalyzes the reversible reaction of succinyl-CoA to...
complex is currently known to be composed of three proteins: heme-oxidized IRP2 ubiquitin ligase 1 (HOIL-1), HOIL-1-interacting protein (HOIP), and Shank-associated...
suggest, contain a heme. The names of the blood oxygen transporters hemoglobin, hemocyanin, and hemerythrin do not refer to the heme group (only found...
Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial (SUCLA2), also known as ADP-forming succinyl-CoA synthetase (SCS-A), is an enzyme that in...
diseases. The heme domain contains an N-terminal loop that binds heme and provides the axial ligands C52 and H65. The distance of heme from the PLP binding...
catabolism, as well as synthesis of other cofactors such as CoA, CoQ and heme groups. One well-known reaction is part of the citric acid cycle (also known...
tetrapyrroles, including chlorophyll, vitamin B12, phycobilins, siroheme, heme, and heme d1. It is converted to sirohydrochlorin via dihydrosirohydrochlorin...
peptides and proteins. It also bonds to and permanently disables (poisons) heme-containing enzymes. It is used as an irreversible inhibitor of the oxygen-evolving...
metal ions and iron–sulfur clusters) or organic compounds (e.g., flavin and heme). These cofactors serve many purposes; for instance, metal ions can help...
binding is carbon monoxide which competes with oxygen for the active site on heme. Carbon monoxide's high affinity may outcompete oxygen in the presence of...
NADH-cytochrome c-reductase, kynurenine hydroxylase and fatty acid Co-A ligase. Disruption of the outer membrane permits proteins in the intermembrane...
Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial is an enzyme that in humans is encoded by the SUCLG2 gene on chromosome 3. This gene encodes...
of fresh body weight) of dietary canavanine because their arginine-tRNA ligase has little, if any, discriminatory capacity. No one has examined experimentally...
to coproporhyrinogen III oxidase (HemN), a radical SAM enzyme involved in heme biosynthesis Detailed mechanistic investigations on two class C radical SAM...
deubiquitylating enzymes, termed UBP1-UBP3, and cloned the first specific E3 ubiquitin ligase, termed UBR1 (in 1990). The latter advance opened a particularly large...
Ikura T, Ikura M, Asahara T, Tokunaga F, Iwai K, Igarashi K (October 2007). "Heme induces ubiquitination and degradation of the transcription factor Bach1"...
this pathway is cytochrome b2, that upon being cleaved will interact with a heme cofactor and become active. The second intermembrane space pathway does not...
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